Fc-Binding Peptides for Antibody Purification
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Solution Overview
Problem
Current antibody-binding molecules lack sufficient molecular diversity and stability, particularly in detecting, purifying, and immobilizing antibodies, due to limitations in binding specificity, affinity, and adaptability to various conditions, and existing techniques for analyzing non-native antibody structures are inefficient.
Innovation Solution
Development of novel polypeptides with specific amino acid sequences that exhibit high binding activity to the Fc region of immunoglobulin G, including those that bind selectively to non-native structures, allowing for efficient detection, purification, and removal of antibodies, and providing enhanced stability under various conditions without requiring cyclization.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If protein A derived from Staphylococcus is used for recovering and purifying antibodies, then binding activity to antibodies is achieved, but stability and production cost are insufficient
Solution Approach 1:
The patent uses short peptide sequences (10-20 amino acids) instead of large protein A molecules. These small peptides are chemically synthesized rather than produced through complex biological systems, making them cheaper and more stable. The peptides can be easily produced by standard peptide synthesis methods without requiring bacterial culture and purification processes.
Solution Approach 2:
The patent identifies and utilizes specific binding motifs within the larger protein A structure. By segmenting the functional binding region into smaller peptide sequences (such as the YDPRTGTWRSSIAYGGG sequence), the invention creates minimal functional units that retain antibody binding capability while eliminating the need for producing entire protein A molecules.
2Adaptability or versatility
If existing antibody-binding peptides are used, then some binding activity is achieved, but molecular diversity is insufficient
Solution Approach 1:
The patent systematically varies parameters of the peptide sequences including amino acid composition, sequence length (10-20 residues), and structural features (linear vs. cyclic). By changing these parameters while maintaining the core binding motif YDPRTGTWRSSIAYGGG, the invention generates a diverse family of peptides with different binding characteristics suitable for various applications.
Solution Approach 2:
The patent develops a universal binding motif that can function in multiple contexts - linear and cyclic forms, different lengths, various amino acid substitutions - all maintaining antibody binding capability. This universal motif can be adapted for different antibody types and application requirements, providing versatility across multiple scenarios.
3Stability of the object's composition
If cyclic peptides with disulfide bonds are used to enhance stability, then binding affinity is improved, but complexity of structure increases
Solution Approach 1:
The patent employs simple linear peptide sequences that do not require complex cyclization or disulfide bond formation. These short linear peptides are chemically simpler to synthesize and handle, yet maintain sufficient stability for their intended applications through their optimized amino acid sequences and appropriate buffer conditions.
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
The novel polypeptides demonstrate high binding affinity and stability, enabling effective detection, purification, and removal of antibodies, including those with non-native structures, and can operate under reductive conditions, improving the efficiency of antibody handling processes.
Implementation Method 1
a polypeptide exhibiting binding activity to an Fc region of immunoglobulin G... wherein the polypeptide comprises an amino acid sequence represented by formula (1)
Data Source
Figure 1(A)~1(F)
Figure 2
Figure 3
AI summary
The invention relates to polypeptides consisting of amino acid sequences represented by the following formulas 1 to 4, which have binding activity to an Fc region of immunoglobulin G and can be favorably used in detecting, purifying, immobilizing or removing an antibody, immunoglobulin G or a protein containing an Fc region of immunoglobulin G, Y-D-P-x-T-G-T-W-R-S-x-[IL] (SEQ ID NO: 1) (1) R-[QRS]-x-x-[GS]-Y-D-P-R-T-G-T-W-R-S-S-I-A-Y-G-G (SEQ ID NO: 10) (2) G-V-V-R-Q-W-S-G-x-x-x-x-x-x-x-x-R-S-S-I-A-Y-G-G (SEQ ID NO: 20) (3) D-A-A-W-H-L-G-E-L-V-W-A-T-Y-Y-D-P-E-T-G-T-W-x-P-D-W-x-x-M (SEQ ID NO: 23) (4) where x represents any amino acid residue; and amino acid residues within the square brackets indicate that any one of the amino acid residues is selected.